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Volumn 26, Issue 4, 1997, Pages 789-797

The outer membrane component, YscC, of the Yop secretion machinery of Yersinia enterocolitica forms a ring-shaped multimeric complex

Author keywords

[No Author keywords available]

Indexed keywords

OUTER MEMBRANE PROTEIN;

EID: 0030716279     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1997.6141981.x     Document Type: Article
Times cited : (192)

References (49)
  • 1
    • 0028124264 scopus 로고
    • YscU, a Yersinia enterocolitica inner membrane protein involved in Yop secretion
    • Allaoui, A., Woestyn, S., Sluiters, C., and Cornelis, G.R. (1994) YscU, a Yersinia enterocolitica inner membrane protein involved in Yop secretion. J Bacteriol 176: 4534-4542.
    • (1994) J Bacteriol , vol.176 , pp. 4534-4542
    • Allaoui, A.1    Woestyn, S.2    Sluiters, C.3    Cornelis, G.R.4
  • 2
    • 0028883418 scopus 로고
    • Mutational analysis of the Yersinia enterocolitica virC operon: Characterization of yscE, F, G, I, J, K, and M for Yop secretion and yscH encoding YopR
    • Allaoui, A., Schulte, R., and Cornelis, G.R. (1995a) Mutational analysis of the Yersinia enterocolitica virC operon: characterization of yscE, F, G, I, J, K, and M for Yop secretion and yscH encoding YopR. Mol Microbiol 18: 343-355.
    • (1995) Mol Microbiol , vol.18 , pp. 343-355
    • Allaoui, A.1    Schulte, R.2    Cornelis, G.R.3
  • 4
    • 0028217290 scopus 로고
    • The IcrB (yscN/U) gene cluster of Yersinia pseudotuberculosis is involved in Yop secretion and shows high homology to the spa gene clusters of Shigella flexneri and Salmonella typhimurium
    • Bergman, T., Erickson, K., Galyov, E., Persson, C., and Wolf-Watz, H. (1994) The IcrB (yscN/U) gene cluster of Yersinia pseudotuberculosis is involved in Yop secretion and shows high homology to the spa gene clusters of Shigella flexneri and Salmonella typhimurium. J Bacteriol 176: 2619-2626.
    • (1994) J Bacteriol , vol.176 , pp. 2619-2626
    • Bergman, T.1    Erickson, K.2    Galyov, E.3    Persson, C.4    Wolf-Watz, H.5
  • 5
    • 0020971311 scopus 로고
    • A rapid alkaline extraction method for the isolation of plasmid DNA
    • Birnboim, H.C. (1983) A rapid alkaline extraction method for the isolation of plasmid DNA. Methods Enzymol 100: 243-255.
    • (1983) Methods Enzymol , vol.100 , pp. 243-255
    • Birnboim, H.C.1
  • 6
    • 0029814613 scopus 로고    scopus 로고
    • Status of YopM and YopN in the Yersinia Yop virulon: YopM of Y.enterocolitica is internalized inside the cytosol of PU5-1.8 macrophages by the YopB,D.N delivery apparatus
    • Boland, A., Sory, M.-P., Iriarte, M., Kerbourch, C., Wattiau, P., and Cornelis, G.R. (1996) Status of YopM and YopN in the Yersinia Yop virulon: YopM of Y.enterocolitica is internalized inside the cytosol of PU5-1.8 macrophages by the YopB,D.N delivery apparatus. EMBO J 15: 5191-5201.
    • (1996) EMBO J , vol.15 , pp. 5191-5201
    • Boland, A.1    Sory, M.-P.2    Iriarte, M.3    Kerbourch, C.4    Wattiau, P.5    Cornelis, G.R.6
  • 7
    • 0030028530 scopus 로고    scopus 로고
    • XpsD, an outer membrane protein required for protein secretion by Xanthomonas campestris pv. campestris, forms a multimer
    • Chen, L.-Y., Chen, D.-Y., Miaw, J., and Hu, N.-T. (1996) XpsD, an outer membrane protein required for protein secretion by Xanthomonas campestris pv. campestris, forms a multimer. J Biol Chem 271: 2703-2707.
    • (1996) J Biol Chem , vol.271 , pp. 2703-2707
    • Chen, L.-Y.1    Chen, D.-Y.2    Miaw, J.3    Hu, N.-T.4
  • 8
    • 0015385368 scopus 로고
    • Non-chromosomal antibiotic resistance in bacteria; genetic transformation of Escherichia coli by R factor DNA
    • Cohen, S.N., Chang, A.C.Y., and Hsu, C.L. (1972) Non-chromosomal antibiotic resistance in bacteria; genetic transformation of Escherichia coli by R factor DNA. Proc Natl Acad Sci USA 69: 2110-2114.
    • (1972) Proc Natl Acad Sci USA , vol.69 , pp. 2110-2114
    • Cohen, S.N.1    Chang, A.C.Y.2    Hsu, C.L.3
  • 9
    • 0016637595 scopus 로고
    • Restriction of DNA in Yersinia enterocolitica detected by recipient ability for a derepressed R factor from Escherichia coli
    • Cornelis, G.R., and Colson, C. (1975) Restriction of DNA in Yersinia enterocolitica detected by recipient ability for a derepressed R factor from Escherichia coli. J Gen Microbiol 87: 285-291.
    • (1975) J Gen Microbiol , vol.87 , pp. 285-291
    • Cornelis, G.R.1    Colson, C.2
  • 10
    • 0031026828 scopus 로고    scopus 로고
    • The Yersinia Yop virulon: A bacterial system for subverting eukaryotic cells
    • Cornelis, G.R., and Wolf-Watz, H. (1997) The Yersinia Yop virulon: a bacterial system for subverting eukaryotic cells. Mol Microbiol 23: 861-867.
    • (1997) Mol Microbiol , vol.23 , pp. 861-867
    • Cornelis, G.R.1    Wolf-Watz, H.2
  • 11
    • 0022898996 scopus 로고
    • Genetic analysis of the plasmid region controlling virulence in Yersinia enterocolitica O:9 by Mini-Mu insertions and lac gene fusions
    • Cornelis, G.R., Sory, M.P., Laroche, Y., and Derclaye, I. (1986) Genetic analysis of the plasmid region controlling virulence in Yersinia enterocolitica O:9 by Mini-Mu insertions and lac gene fusions. Microb Pathogen 1: 349-359.
    • (1986) Microb Pathogen , vol.1 , pp. 349-359
    • Cornelis, G.R.1    Sory, M.P.2    Laroche, Y.3    Derclaye, I.4
  • 12
    • 0023255341 scopus 로고
    • Transcription of the yop regulon from Y. enterocolitica requires trans acting pYV and chromosomal genes
    • Cornelis, G.R., Vanooteghem, J.-C., and Sluiters, C. (1987) Transcription of the yop regulon from Y. enterocolitica requires trans acting pYV and chromosomal genes. Microb Pathogen 2: 367-379.
    • (1987) Microb Pathogen , vol.2 , pp. 367-379
    • Cornelis, G.R.1    Vanooteghem, J.-C.2    Sluiters, C.3
  • 13
    • 0024546348 scopus 로고
    • Homology between VirF, the transcriptional activator of the Yersinia virulence regulon, and AraC, the Escherichia coli arabinose operon regulator
    • Cornelis, G., Sluiters, C., Lambert de Rouvrait, C., and Michiels, T. (1989) Homology between VirF, the transcriptional activator of the Yersinia virulence regulon, and AraC, the Escherichia coli arabinose operon regulator. J Bacteriol 171: 254-262.
    • (1989) J Bacteriol , vol.171 , pp. 254-262
    • Cornelis, G.1    Sluiters, C.2    Lambert De Rouvrait, C.3    Michiels, T.4
  • 15
    • 0028178610 scopus 로고
    • 2+ response (LCR) secretion (ysc) locus lies within the IcrB region of the LCR plasmid in Yersinia pestis
    • 2+ response (LCR) secretion (ysc) locus lies within the IcrB region of the LCR plasmid in Yersinia pestis. J Bacteriol 176: 569-579.
    • (1994) J Bacteriol , vol.176 , pp. 569-579
    • Fields, K.A.1    Piano, G.V.2    Straley, S.C.3
  • 16
    • 0028031879 scopus 로고
    • Regulation and polarized transfer of the Yersinia outer proteins (Yops) involved in antiphagocytosis
    • Forsberg, Å., Rosqvist, R., and Wolf-Watz, H. (1994) Regulation and polarized transfer of the Yersinia outer proteins (Yops) involved in antiphagocytosis. Trends Microbiol 2: 14-19.
    • (1994) Trends Microbiol , vol.2 , pp. 14-19
    • Forsberg, Å.1    Rosqvist, R.2    Wolf-Watz, H.3
  • 17
    • 0025762461 scopus 로고
    • The surface-located YopN protein is involved in calcium signal transduction in Yersinia pseudotuberculoses
    • Forsberg, Å., Viitanen, A.M., Skurnik, M., and Wolf-Watz, H. (1991) The surface-located YopN protein is involved in calcium signal transduction in Yersinia pseudotuberculoses. Mol Microbiol 5: 977-986.
    • (1991) Mol Microbiol , vol.5 , pp. 977-986
    • Forsberg, Å.1    Viitanen, A.M.2    Skurnik, M.3    Wolf-Watz, H.4
  • 18
    • 0022870839 scopus 로고
    • Molecular cloning of the plasmid RP4 primase region in a multi-host-range tacP expression vector
    • Fürste, J.P., Pansegrau, W., Frank, R., Blöcker, H., Scholz, P., Bagdasarian, M., and Lanka, E. (1986) Molecular cloning of the plasmid RP4 primase region in a multi-host-range tacP expression vector. Gene 48: 119-131.
    • (1986) Gene , vol.48 , pp. 119-131
    • Fürste, J.P.1    Pansegrau, W.2    Frank, R.3    Blöcker, H.4    Scholz, P.5    Bagdasarian, M.6    Lanka, E.7
  • 19
    • 0029879556 scopus 로고    scopus 로고
    • Molecular genetic bases of Salmonella entry into host cells
    • Galan, J.E. (1996) Molecular genetic bases of Salmonella entry into host cells. Mol Microbiol 20: 263-271.
    • (1996) Mol Microbiol , vol.20 , pp. 263-271
    • Galan, J.E.1
  • 20
    • 0028353854 scopus 로고
    • A superfamily of proteins involved in different secretion pathways in gram-negative bacteria: Modular structure and specificity of the N-terminal domain
    • Genin, S., and Boucher, C.A. (1994) A superfamily of proteins involved in different secretion pathways in gram-negative bacteria: modular structure and specificity of the N-terminal domain. Mol Gen Genet 243: 112-118.
    • (1994) Mol Gen Genet , vol.243 , pp. 112-118
    • Genin, S.1    Boucher, C.A.2
  • 21
    • 0031047135 scopus 로고    scopus 로고
    • Functional analysis of exsC and exsB in regulation of exoenzyme S production by Pseudomonas aeruginosa
    • Goranson, J., Hovey, A.K., and Frank, D.W. (1997) Functional analysis of exsC and exsB in regulation of exoenzyme S production by Pseudomonas aeruginosa. J Bacteriol 179: 1646-1654.
    • (1997) J Bacteriol , vol.179 , pp. 1646-1654
    • Goranson, J.1    Hovey, A.K.2    Frank, D.W.3
  • 22
    • 0020959710 scopus 로고
    • Studies on transformation of E. coli with plasmids
    • Hanahan, D. (1983) Studies on transformation of E. coli with plasmids. J Mol Biol 166: 557-580.
    • (1983) J Mol Biol , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 23
    • 0018074492 scopus 로고
    • Outer membranes of Gram-negative bacteria
    • Hancock, R.E.W., and Nikaido, H. (1978) Outer membranes of Gram-negative bacteria. J Bacteriol 136: 381-390.
    • (1978) J Bacteriol , vol.136 , pp. 381-390
    • Hancock, R.E.W.1    Nikaido, H.2
  • 24
    • 0029870545 scopus 로고    scopus 로고
    • Insertion of an outer membrane protein in Escherichia coli requires a chaperone-like protein
    • Hardie, K.R., Lory, S., and Pugsley, A.P. (1996a) Insertion of an outer membrane protein in Escherichia coli requires a chaperone-like protein. EMBO J 15: 978-988.
    • (1996) EMBO J , vol.15 , pp. 978-988
    • Hardie, K.R.1    Lory, S.2    Pugsley, A.P.3
  • 25
    • 10544256597 scopus 로고    scopus 로고
    • The secretin-specific, chaperone-like protein of the general secretory pathway: Separation of proteolytic protection and piloting functions
    • Hardie, K.R., Seydel, A., Guilvout, I., and Pugsly, A.P. (1996b) The secretin-specific, chaperone-like protein of the general secretory pathway: separation of proteolytic protection and piloting functions. Mol Microbiol 22: 967-976.
    • (1996) Mol Microbiol , vol.22 , pp. 967-976
    • Hardie, K.R.1    Seydel, A.2    Guilvout, I.3    Pugsly, A.P.4
  • 26
    • 0025837193 scopus 로고
    • A wide-host-range suicide vector for improving reverse genetics in gram-negative bacteria: Inactivation of the bla gene of Yersinia enterocolitica
    • Kaniga, K., Delor, I., and Cornelis, G.R. (1991) A wide-host-range suicide vector for improving reverse genetics in gram-negative bacteria: inactivation of the bla gene of Yersinia enterocolitica. Gene 109: 137-141.
    • (1991) Gene , vol.109 , pp. 137-141
    • Kaniga, K.1    Delor, I.2    Cornelis, G.R.3
  • 27
    • 0029875905 scopus 로고    scopus 로고
    • Essential role of a sodium dodecyl sulfate-resistant protein pIV multimer in assembly export of filamentous phage
    • Linderoth, N.A., Model, P., and Russel, M. (1996) Essential role of a sodium dodecyl sulfate-resistant protein pIV multimer in assembly export of filamentous phage. J Bacteriol 178: 1962-1970.
    • (1996) J Bacteriol , vol.178 , pp. 1962-1970
    • Linderoth, N.A.1    Model, P.2    Russel, M.3
  • 28
    • 0016841078 scopus 로고
    • Electrophoretic resolution of the 'major outer membrane protein' of Escherichia coli K12 into four bands
    • Lugtenberg, B., Meyers, J.M., Peters, M., van der Hoek, P., and Alphen, L. (1975) Electrophoretic resolution of the 'major outer membrane protein' of Escherichia coli K12 into four bands. FEBS Lett 58: 254-258.
    • (1975) FEBS Lett , vol.58 , pp. 254-258
    • Lugtenberg, B.1    Meyers, J.M.2    Peters, M.3    Van Der Hoek, P.4    Alphen, L.5
  • 29
    • 0027244956 scopus 로고
    • Non-polar mutagenesis of the ipa genes defines IpaB, IpaC, and IpaD as effectors of Shigella flexneri entry into epithelial cells
    • Menard, R., Sansonetti, P.J., and Parsot, C. (1993) Non-polar mutagenesis of the ipa genes defines IpaB, IpaC, and IpaD as effectors of Shigella flexneri entry into epithelial cells. J Bacteriol 175: 5899-5906.
    • (1993) J Bacteriol , vol.175 , pp. 5899-5906
    • Menard, R.1    Sansonetti, P.J.2    Parsot, C.3
  • 30
    • 0030003139 scopus 로고    scopus 로고
    • Bacterial entry into epithelial cells: The paradigm of Shigella
    • Menard, R., Dehio, C., and Sansonetti, P.J. (1996) Bacterial entry into epithelial cells: the paradigm of Shigella. Trends Microbiol 4: 220-225.
    • (1996) Trends Microbiol , vol.4 , pp. 220-225
    • Menard, R.1    Dehio, C.2    Sansonetti, P.J.3
  • 31
    • 0026065361 scopus 로고
    • Secretion of hybrid proteins by the Yersinia Yop export system
    • Michiels, T., and Cornelis, G.R. (1991) Secretion of hybrid proteins by the Yersinia Yop export system. J Bacteriol 173: 1677-1685.
    • (1991) J Bacteriol , vol.173 , pp. 1677-1685
    • Michiels, T.1    Cornelis, G.R.2
  • 34
    • 0023892552 scopus 로고
    • A novel suicide vector and its use in construction of insertion mutations; osmoregulation of outer membrane proteins and virulence determinants in Vibrio cholerae requires ToxR
    • Miller, V.L., and Mekalanos, J.J. (1988) A novel suicide vector and its use in construction of insertion mutations; osmoregulation of outer membrane proteins and virulence determinants in Vibrio cholerae requires ToxR. J Bacteriol 170: 2575-2583.
    • (1988) J Bacteriol , vol.170 , pp. 2575-2583
    • Miller, V.L.1    Mekalanos, J.J.2
  • 35
    • 0018866264 scopus 로고
    • High-molecular-weight antigenic protein complex in the outer membrane of Neisseria gonorrhoeae
    • Newhall, W.J., Wilde III, C.E., Sawyer, W.D., and Haak, R.A. (1980) High-molecular-weight antigenic protein complex in the outer membrane of Neisseria gonorrhoeae. Infect Immun 27: 475-482.
    • (1980) Infect Immun , vol.27 , pp. 475-482
    • Newhall, W.J.1    Wilde III, C.E.2    Sawyer, W.D.3    Haak, R.A.4
  • 37
    • 0027297680 scopus 로고
    • Multiple effects of IcrD mutations in Yersinia pestis
    • Piano, G.V., and Straley, S.C. (1993) Multiple effects of IcrD mutations in Yersinia pestis. J Bacteriol 175: 3536-3545.
    • (1993) J Bacteriol , vol.175 , pp. 3536-3545
    • Piano, G.V.1    Straley, S.C.2
  • 38
    • 0029039020 scopus 로고
    • Mutations in yscC, yscD, and yscG prevent high-level expression and secretion of V-antigen and Yops in Yersinia pestis
    • Piano, G.V., and Straley, S.C. (1995) Mutations in yscC, yscD, and yscG prevent high-level expression and secretion of V-antigen and Yops in Yersinia pestis. J Bacteriol 177: 3843-3854.
    • (1995) J Bacteriol , vol.177 , pp. 3843-3854
    • Piano, G.V.1    Straley, S.C.2
  • 39
    • 0027982852 scopus 로고
    • Target cell contact triggers expression and polarized transfer of Yersinia YopE cytotoxin into mammalian cells
    • Rosqvist, R., Magnusson, K., and Wolf-Watz, H. (1994) Target cell contact triggers expression and polarized transfer of Yersinia YopE cytotoxin into mammalian cells. EMBO J 13: 964-972.
    • (1994) EMBO J , vol.13 , pp. 964-972
    • Rosqvist, R.1    Magnusson, K.2    Wolf-Watz, H.3
  • 40
    • 0027982566 scopus 로고
    • Phage assembly, a paradigm for bacterial virulence factor export?
    • Russel, M. (1994) Phage assembly, a paradigm for bacterial virulence factor export? Science 265: 612-614.
    • (1994) Science , vol.265 , pp. 612-614
    • Russel, M.1
  • 42
    • 0028929450 scopus 로고
    • The bacterial flagellum: From genetic network to complex architecture
    • Shapiro, L. (1995) The bacterial flagellum: from genetic network to complex architecture. Cell 80: 525-527.
    • (1995) Cell , vol.80 , pp. 525-527
    • Shapiro, L.1
  • 43
    • 0030911423 scopus 로고    scopus 로고
    • Specific interaction between OutD, an Erwinia chrysanthemi outer membrane protein of the general secretory pathway, and secreted proteins
    • Shevchik, V.E., Robert-Baudouy, J., and Condemine, G. (1997) Specific interaction between OutD, an Erwinia chrysanthemi outer membrane protein of the general secretory pathway, and secreted proteins. EMBO J 16: 3007-3016.
    • (1997) EMBO J , vol.16 , pp. 3007-3016
    • Shevchik, V.E.1    Robert-Baudouy, J.2    Condemine, G.3
  • 44
    • 0029608720 scopus 로고
    • Identification of the YopE and YopH domains required for secretion and internalization into the cytosol of macrophages, using the cyaA gene fusion approach
    • Sory, M.-P., Boland, A., Lambermont, L, and Cornelis, G.R. (1995) Identification of the YopE and YopH domains required for secretion and internalization into the cytosol of macrophages, using the cyaA gene fusion approach. Proc Natl Acad Sci USA 92: 11998-12002.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 11998-12002
    • Sory, M.-P.1    Boland, A.2    Lambermont, L.3    Cornelis, G.R.4
  • 45
    • 0025976068 scopus 로고
    • Carboxy-terminal phenylalanine is essential for the correct assembly of a bacterial outer membrane protein
    • Struyvé, M., Moons, M., and Tommassen, J. (1991) Carboxy-terminal phenylalanine is essential for the correct assembly of a bacterial outer membrane protein. J Mol Biol 218: 141-148.
    • (1991) J Mol Biol , vol.218 , pp. 141-148
    • Struyvé, M.1    Moons, M.2    Tommassen, J.3
  • 46
    • 0027250857 scopus 로고
    • Conservation of secretion pathways for pathogenicity determinants of plant and animal bacteria
    • Van Gijsegem, F., Genin, S., and Boucher, C.A. (1993) Conservation of secretion pathways for pathogenicity determinants of plant and animal bacteria. Trends Microbiol 1: 175-180.
    • (1993) Trends Microbiol , vol.1 , pp. 175-180
    • Van Gijsegem, F.1    Genin, S.2    Boucher, C.A.3
  • 47
    • 0026737314 scopus 로고
    • Structure of porin refined at 1.8 Å resolution
    • Weiss, M.S., and Schulz, G.E. (1992) Structure of porin refined at 1.8 Å resolution. J Mol Biol 227: 493-509.
    • (1992) J Mol Biol , vol.227 , pp. 493-509
    • Weiss, M.S.1    Schulz, G.E.2
  • 48
    • 0028292926 scopus 로고
    • YscN, the putative energizer of the Yersinia Yop secretion machinery
    • Woestyn, S., Allaoui, A., Wattiau, P., and Cornelis, G.R. (1994) YscN, the putative energizer of the Yersinia Yop secretion machinery. J Bacteriol 176: 1561-1569.
    • (1994) J Bacteriol , vol.176 , pp. 1561-1569
    • Woestyn, S.1    Allaoui, A.2    Wattiau, P.3    Cornelis, G.R.4
  • 49
    • 0029801248 scopus 로고    scopus 로고
    • Exoenzyme S of Pseudomonas aeruginosa is secreted by a type III pathway
    • Yahr, T.L., Goranson, J., and Frank, D.W. (1996) Exoenzyme S of Pseudomonas aeruginosa is secreted by a type III pathway. Mol Microbiol 22: 991-1003.
    • (1996) Mol Microbiol , vol.22 , pp. 991-1003
    • Yahr, T.L.1    Goranson, J.2    Frank, D.W.3


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